Rhodopsins visual pigments

The visual pigment present in rods has been termed rhodopsin and consists of 11-m-retinal, a derivative of vitamin A1( and a lipoprotein called opsin. Recent evidence(43) suggests that in native rhodopsin the retinal chromo-phore is covalently bonded to a phosphatidylethanolamine residue of the lipid portion of opsin. The structure of 1 l-cis-retinal is as follows ... 

Rhodopsin is a seven ot-helix trans-membrane protein and visual pigment of the vertebrate rod photoreceptor cells that mediate dim light vision. In this photoreceptor, retinal is the chromophore bound by opsin protein, covalently linked to Lys296 by a Schiff base linkage. Kpega et al.64 have studied NMR spectra of Schiff bases being derivatives of all-frans retinal and amino-p-cyclodextrins as a model of rhodopsin, where p-cyclodextrin plays a role of a binding pocket. On the basis of analysis of the chemical shift differences for the model compound in the presence and in the absence of adamantane carboxylate, it has been shown that the derivative of 3-amino-p-cyclodextrin forms dimer in water and retinoid is inserted into p-cyclodextrin cavity [31]. 

Intriguingly, the conical intersection model also suggests that E,Z-isomerization of acyclic dienes might be accompanied by conformational interconversion about the central bond, reminiscent of the so-called Hula-Twist mechanism for the efficient ,Z-photo-isomerization of the visual pigment rhodopsin in its rigid, natural protein environment101. A study of the photochemistry of deuterium-labelled 2,3-dimethyl-l,3-butadiene (23-d2) in low temperature matrices (vide infra) found no evidence for such a mechanism in aliphatic diene E,Z -photoisomerizations102. On the other hand, Fuss and coworkers have recently reported results consistent with the operation of this mechanism in the E,Z-photoisomerization of previtamin D3 (vide infra)103. 

A deficiency of vitamin A leads to vision defects, including a visual impairment at low light levels, termed night blindness. For the processes of vision, retinol needs to be converted first by oxidation into the aldehyde retinal, and then by enzymic isomerization to cw-retinal. c -Retinal is then bound to the protein opsin in the retina via an imine linkage (see Section 7.7.1) to give the red visual pigment rhodopsin. 

The light absorption of rhodopsin is in the visible range, with a maximum at about 500 nm. The absorption properties of the visual pigment are thus optimally adjusted to the spectral distribution of sunlight. 

Lucas RJ, Douglas RH, Foster RG 2001 Characterization of an ocular photopigment capable of driving pupillary constriction in mice. Nat Neurosci 4 621—626 Lythgoe JN, Shand J, Foster RG 1984 Visual pigment in fish iridocytes. Nature 308 83—84 Menon ST, Han M, Sakmar TP 2001 Rhodopsin structural basis of molecular physiology. Physiol Rev 81 1659-1688... 

Spectroscopy and Physical Chemistry of Retinal and Visual Pigments. Several reviews and symposium proceedings discuss the spectroscopic, photochemical, or physicochemical properties of retinal and related compounds, and of natural and model visual pigments derived from them. " " In addition, many papers have been published dealing with specific aspects of the spectroscopy (u.v., n.m.r., resonance Raman) of retinals and rhodopsins" or with aspects of the photochemistry and physical chemistry of retinal derivatives which may be relevant to the functioning of rhodopsin and other visual pigments. The bacterial purple... 

Photochemical cis-trans isomerization in a conjugated polyene system is thought to be the crucial primary process in vision. The visual pigment (rhodopsin) is derived from 11 -crs-retinal by reaction of the aldehyde group with an amino substituent in a protein (opsin). There is considerable distortion in the geometry of this chromophoric group anyway, because of the spatial requirements of the protein... 

The Visual Pigments Are Found in Rod and Cone Cells Rhodopsin Consists of 11-cri-Retinal Bound to the... 

Partridge, J. De Grip, W. (1991) A new template for rhodopsin (vitamin A, based) visual pigments Vision Renvoi. 31, pp 619-630... 

Tokunaga, F. et. al. (1999) Evolution of visual pigments and related molecules. In rhodopsins and phototransduction. NY John Wiley Sons. pp. 44-53... 

Vitamin A, or retinol, is one of the major fat-soluble vitamins. It is present in many foods the best natural sources are liver, butter, margarine, egg yolk, carrots, spinach, and sweet potatoes. Vitamin A is the precursor of retinal, the essential component of the visual pigment rhodopsin. 

A double bond in rhodopsin, a visual pigment found in your eyes that enables you to see at night, is converted from the cis isomerto the trans isomer when light strikes the eye. As a result, a nerve impulse travels to the brain and you see the source of the light. 

Retinal as Visual Pigment Model Spectroscopy and Physical Chemistry. Several theoretical, spectroscopic, and photochemical studies aimed at correlating the behaviour of retinal and derivatives, especially Schiff s bases, with that of rhodopsin and related visual pigments have been reported.95-104 A review of recent work in this field has been presented.105... 

The opsin consists of protein (ca. 80-85% of which is rhodopsin), phospholipids and carbohydrates and contains very little cholesterol (1-3%) (for a review, see [6]). While the molecular weight (e.g., 40000 for bovine rhodopsin) [7], carbohydrate [8,9], lipid and amino acid [10-12] composition have been established for some rhodopsins, there is as yet no example of a visual pigment for which the full amino acid sequence is known. Only a quarter of about the 300 residues of rhodopsin have been sequenced [13,14], 39 residues at the N-terminus and 40 residues at the C-terminus. The structure of the moiety containing retinal, i.e., retinal-lysine-alanine, which is located in the carboxy-terminal region has, however, been elucidated ([15] see also [78] and references therein). The N-terminal residue was identified as acetylmethionine [16]. 

Visual pigments display characteristic absorption spectra which result from the very specific interactions between protein and chromophore in the binding site, i.e., the absorbance spectrum of retinal at ca. 380 nm is red-shifted to ca. 500 nm in bovine rhodopsin. However, depending on species, rhodopsins absorb from 440 to ca. 600 nm. Porphyropsins show a similar spread in their absorption maxima, absorb at longer wavelengths than the corresponding rhodopsins, and have lower extinction coefficients (ca. 75%) than rhodopsins (e.g., bovine rhodopsin e, ca. 40500) [17] as shown in Fig. 2. 

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